Selenolthiol and dithiol C-terminal tetrapeptide motifs for one-step purification and labeling of recombinant proteins produced in E. coli. (Q54454031)

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20 December 2019

title

Selenolthiol and dithiol C-terminal tetrapeptide motifs for one-step purification and labeling of recombinant proteins produced in E. coli (English)

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20 December 2019

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1

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20 December 2019

Elias Arnér

7

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20 December 2019

author name string

Linda Johansson

2

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20 December 2019

Jan-Olov Thorell

3

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20 December 2019

Anna Fredriksson

4

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20 December 2019

Erik Samén

5

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Sharon Stone-Elander

6

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publication date

1 December 2006

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20 December 2019

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volume

7

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20 December 2019

issue

12

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20 December 2019

page(s)

1976-1981

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Selenocysteine: the 21st amino acid

20 December 2019

cites work

1 reference

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Selenocysteine in proteins-properties and biotechnological use.

21 January 2018

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Recombinant expression of mammalian selenocysteine-containing thioredoxin reductase and other selenoproteins in Escherichia coli

21 January 2018

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High-level expression in Escherichia coli of selenocysteine-containing rat thioredoxin reductase utilizing gene fusions with engineered bacterial-type SECIS elements and co-expression with the selA, selB and selC genes

21 January 2018

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Mammalian thioredoxin reductase: oxidation of the C-terminal cysteine/selenocysteine active site forms a thioselenide, and replacement of selenium with sulfur markedly reduces catalytic activity

21 January 2018

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Structure and mechanism of mammalian thioredoxin reductase: the active site is a redox-active selenolthiol/selenenylsulfide formed from the conserved cysteine-selenocysteine sequence

21 January 2018

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Exploiting the 21st amino acid-purifying and labeling proteins by selenolate targeting.

21 January 2018

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Tagging recombinant proteins with a Sel-tag for purification, labeling with electrophilic compounds or radiolabeling with 11C.

21 January 2018

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Substitution of the thioredoxin system for glutathione reductase in Drosophila melanogaster

21 January 2018

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Active sites of thioredoxin reductases: why selenoproteins?

21 January 2018

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Formation of disulfide bonds and homodimers of the major cat allergen Fel d 1 equivalent to the natural allergen by expression in Escherichia coli.

21 January 2018

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The crystal structure of the major cat allergen Fel d 1, a member of the secretoglobin family

21 January 2018

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Assessment of production conditions for efficient use of Escherichia coli in high-yield heterologous recombinant selenoprotein synthesis.

21 January 2018

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1-[3-(2-[18F]fluoropyridin-3-yloxy)propyl]pyrrole-2,5-dione: design, synthesis, and radiosynthesis of a new [18F]fluoropyridine-based maleimide reagent for the labeling of peptides and proteins.

21 January 2018

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A mouse model for in vivo tracking of the major dust mite allergen Der p 2 after inhalation

21 January 2018

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11C-labeled 4-isopropylantipyrine: preparation and biological evaluation as a blood flow tracer in positron emission tomography (PET).

21 January 2018

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21 January 2018

Identifiers

DOI

10.1002/CBIC.200600326

1 reference

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20 December 2019

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